Storage and secretion of Ag-Aper14, a novel peritrophic matrix protein, and Ag-Muc1 from the mosquito Anopheles gambiae

• Published in: Cell and tissue research Vol. 320; no. 1; pp. 175 - 185
• Main Authors: Devenport, M, Fujioka, H, Donnelly-Doman, M, Shen, Z, Jacobs-Lorena, M
• Format: Journal Article
• Language: English
• Published: Germany Springer-Verlag 01-04-2005; Springer Nature B.V
• Subjects: Amino Acid Sequence; amino acids; Animals; Anopheles - metabolism; Anopheles gambiae; Antibodies - metabolism; Base Sequence; blood; Digestive System - metabolism; Digestive System - secretion; Digestive System - ultrastructure; epithelial cells; Epithelium - metabolism; Epithelium - secretion; Female; genes; Insect Proteins - chemistry; Insect Proteins - genetics; Insect Proteins - metabolism; Insect Proteins - secretion; Larva; microscopy; Molecular Sequence Data; peritrophic membrane; Protein Structure, Tertiary; secretion; secretory granules; Sequence Homology, Amino Acid
• ISSN: 0302-766X; 1432-0878
• DOI: 10.1007/s00441-004-1067-3

The gene Ag-Aper14 encodes a novel peritrophic matrix (or peritrophic membrane; PM) protein in the mosquito Anopheles gambiae. The Ag-Aper14 protein is merely 89 amino acids long and has a single putative chitin-binding domain. Prior to blood feeding, the Ag-Aper14 protein is stored in secretory vesicles next to the epithelial cell lumenal surface. Immunoelectron microscopy has revealed that Ag-Aper14 co-localizes to the same secretory vesicles as another PM protein, Ag-Aper1, indicating a common mode of regulated secretion. Conversely, Ag-Muc1, an epithelial cell-surface protein, does not co-localize to these secretory vesicles and is detected only on the cell surface. After blood feeding, Ag-Aper14 is secreted and incorporated into the PM that surrounds the ingested blood.